[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0167-4781(92)90102-6; PubMed=1581363 [NCBI, ExPASy, EBI, Israel, Japan] Fitzgerald G.F., Hutchison W.M., Dahl H.H.M.; "Isolation and characterisation of the mouse pyruvate dehydrogenase E1 alpha genes."; Biochim. Biophys. Acta 1131:83-90(1992).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=FVB/N; TISSUE=Mammary gland; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	PROTEIN SEQUENCE OF 46-58; 120-127; 133-141; 216-244; 246-263; 268-274; 278-321; 324-343 AND 379-385, AND MASS SPECTROMETRY. STRAIN=C57BL/6; TISSUE=Brain; Lubec G., Kang S.U.; Submitted (APR-2007) to UniProtKB.
[4]	PROTEIN SEQUENCE OF 159-182; 216-226 AND 278-302, AND MASS SPECTROMETRY. TISSUE=Hippocampus; Lubec G., Klug S.; Submitted (MAR-2007) to UniProtKB.
[5]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, AND MASS SPECTROMETRY. TISSUE=Brain; DOI=10.1074/jbc.M411220200; PubMed=15572359 [NCBI, ExPASy, EBI, Israel, Japan] Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G.; "Proteomic analysis of in vivo phosphorylated synaptic proteins."; J. Biol. Chem. 280:5972-5982(2005).
[6]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-301, AND MASS SPECTROMETRY. TISSUE=Brain; DOI=10.1021/pr0701254; PubMed=18034455 [NCBI, ExPASy, EBI, Israel, Japan] Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."; J. Proteome Res. 7:311-318(2008).
[7]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-293 AND SER-300, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1074/mcp.M600218-MCP200; PubMed=17208939 [NCBI, ExPASy, EBI, Israel, Japan] Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.; "Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS."; Mol. Cell. Proteomics 6:669-676(2007).
[8]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; TYR-289; SER-293 AND SER-300, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1073/pnas.0609836104; PubMed=17242355 [NCBI, ExPASy, EBI, Israel, Japan] Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; "Large-scale phosphorylation analysis of mouse liver."; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).

Comments

FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO₂.
COFACTOR: Thiamine pyrophosphate.
ENZYME REGULATION: E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit.
SUBUNIT: Tetramer of 2 alpha and 2 beta subunits.
SUBCELLULAR LOCATION: Mitochondrion matrix.
TISSUE SPECIFICITY: In all tissues, but in very low amount in testis.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M76727; AAA53046.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007142; AAH07142.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S23506; S23506.

NP_032836.1; -.

3D structure databases

HSSP

P08559; 1NI4. [HSSP ENTRY / PDB]

P35486; 29-390.

PTM databases

P35486; -.

2D gel databases

REPRODUCTION-2DPAGE

P35486; -.

Organism-specific databases

MGI

MGI:97532; Pdha1.

Gene expression databases

ArrayExpress

P35486; -.

CleanEx

MM_PDHA1; -.

GermOnline

ENSMUSG00000031299; Mus musculus.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004739;	Molecular function: pyruvate dehydrogenase (acetyl-transferring) activity (inferred from electronic annotation from EC).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001017; DHase_E1.
IPR017597; Pyrv_DH_E1_asu_subgrp-y.
Graphical view of domain structure.

Pfam

PF00676; E1_dh; 1.
Pfam graphical view of domain structure.

ProtoNet

P35486.

Genome annotation databases

Ensembl

ENSMUSG00000031299; Mus musculus. [Contig view]

GeneID

18597; -.

KEGG

mmu:18597; -.

Phylogenomic databases

HOGENOM

P35486; -.

HOVERGEN

P35486; -.

Other

NextBio

294490; -.

SOURCE

Pdha1; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Glycolysis; Mitochondrion; Oxidoreductase; Phosphoprotein; Pyruvate; Thiamine pyrophosphate; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 29`	`29`	`Mitochondrion (By similarity).`
`CHAIN`	`30 390`	`361`	`Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial.`	`PRO_0000020442`
`MOD_RES`	`232 232`		`Phosphoserine.`
`MOD_RES`	`289 289`		`Phosphotyrosine.`
`MOD_RES`	`293 293`		`Phosphoserine.`
`MOD_RES`	`295 295`		`Phosphoserine (By similarity).`
`MOD_RES`	`300 300`		`Phosphoserine.`
`MOD_RES`	`301 301`		`Phosphotyrosine.`

Sequence information

Length: 390 AA [This is the length of the unprocessed precursor]

Molecular weight: 43232 Da [This is the MW of the unprocessed precursor]

CRC64: 40898944CE8E0A03 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRKMLAAVSR VLAGSAQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED 

        70         80         90        100        110        120 
GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA 

       130        140        150        160        170        180 
HGFTFTRGLP VRAILAELTG RRGGCAKGKG GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA 

       190        200        210        220        230        240 
CKYNGKDEVC LTLYGDGAAN QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST 

       250        260        270        280        290        300 
DYYKRGDFIP GLRVDGMDIL CVREATKFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS 

       310        320        330        340        350        360 
YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA QFATADPEPP 

       370        380        390 
LEELGYHIYS SDPPFEVRGA NQWIKFKSVS

P35486 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools